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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-1-4
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pubmed:abstractText |
Methanediphosphonate and 12 analogs thereof with different substituents at the carbon atom are potent competitive inhibitors of highly purified rat liver and bovine heart inorganic pyrophosphatases. The inhibition constants for the most effective diphosphonates, which contain an NH2 or OH group at the bridge carbon atom, are in the micromolar range. Yeast and Escherichia coli pyrophosphatases are markedly less sensitive to the diphosphonates. Pyrophosphatase inhibition may be related to the numerous biological effects exerted by diphosphonates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
280-4
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:2848451-Animals,
pubmed-meshheading:2848451-Cattle,
pubmed-meshheading:2848451-Cytoplasm,
pubmed-meshheading:2848451-Diphosphonates,
pubmed-meshheading:2848451-Escherichia coli,
pubmed-meshheading:2848451-Liver,
pubmed-meshheading:2848451-Myocardium,
pubmed-meshheading:2848451-Pyrophosphatases,
pubmed-meshheading:2848451-Rats,
pubmed-meshheading:2848451-Saccharomyces cerevisiae,
pubmed-meshheading:2848451-Species Specificity,
pubmed-meshheading:2848451-Structure-Activity Relationship
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pubmed:year |
1988
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pubmed:articleTitle |
Diphosphonates are potent inhibitors of mammalian inorganic pyrophosphatase.
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pubmed:affiliation |
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
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pubmed:publicationType |
Journal Article
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